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NEK1 phosphorylates PP1gamma, leading to the dephosphorylation of WAPL, which, in turn, results in its retention on chromosome cores to promote loss of cohesion at the end of prophase I in mammals.
The interaction between PPP1CC2 and AKAP4 (show AKAP4 ELISA Kits) in human spermatozoa.
Aurkb (show AURKB ELISA Kits) phosphorylates Oct4 (show POU5F1 ELISA Kits)(S229) during G2/M phase, leading to the dissociation of Oct4 (show POU5F1 ELISA Kits) from chromatin, whereas PP1 binds Oct4 (show POU5F1 ELISA Kits) and dephosphorylates Oct4 (show POU5F1 ELISA Kits)(S229) during M/G1 transition, which resets Oct4 (show POU5F1 ELISA Kits)-driven transcription for pluripotency and the cell cycle.
avidity for the substrate plays an important role in imparting specificity on the PPP1R15B-PP1G-actin ternary complex.
PP1 directly interacts with IRF3 (show IRF3 ELISA Kits) and dephosphorylates IRF3 (show IRF3 ELISA Kits) at Ser385 and Ser396, resulting in the suppression of TLR- and RLR (show DHX58 ELISA Kits)-triggered IFN-beta (show IFNB1 ELISA Kits) production.
The endogenous Ppp1cc promoter normally functions in the testis to maintain a sufficient level of PPP1CC2 expression for normal spermatogenesis to occur.
In mouse testis, PPP1CC2 can form a complex with TSSK1 (show TSSK1B ELISA Kits) mediated by the direct interaction of each with the kinase substrate protein TSKS (show TSKS ELISA Kits). Interaction between PPP1CC2 and TSKS (show TSKS ELISA Kits) is mediated through an RVxF docking motif on the TSKS (show TSKS ELISA Kits) surface.
Spermatogenic defects observed in the global Ppp1cc knockout mice and in mice expressing low levels of PPP1CC2 in testis are due to compromised functions of PPP1CC2 in meiotic and postmeiotic germ cells.
The present study focused on TGF-beta-modulation of paxillin and the serine/threonine protein phosphatase PP-1, and the impact on cellular motility.
Results identify protein phosphatase 1 (PP1) as regulator of period and light-induced resetting of the mammalian circadian clock.
Here the authors show how Ki-67 (show MKI67 ELISA Kits) and RepoMan form mitotic exit phosphatases by recruiting PP1 (show PPA1 ELISA Kits), how they distinguish between distinct PP1 (show PPA1 ELISA Kits) isoforms and how the assembly of these two holoenzymes are dynamically regulated by Aurora B kinase (show AURKB ELISA Kits) during mitosis.
Data suggest that PPP1CC catalyzes hydrolysis of an assortment of substrates (aryl methylphosphonates, fluorophosphate esters, phosphorothioate esters, phosphodiesters); conservative mutation of R221 to K results in a mutant that is more effective catalyst toward monoanionic substrates; PPP1CC does not catalyze the hydrolysis of a sulfate ester, which is unexpected.
PP1gamma is upregulated in hepatocellular carcinoma (HCC (show FAM126A ELISA Kits)) cell lines and HCC (show FAM126A ELISA Kits) specimens and promotes cancer cell proliferation through regulation of p53 (show TP53 ELISA Kits). High expression of PP1gamma in HCC (show FAM126A ELISA Kits) cells contributed to doxorubicin resistance.
knock-down of PP1gamma alleviates glioma proliferation by reducing p65 (show GORASP1 ELISA Kits) transportation into the nucleus.
Although no obvious defects in the progression of mitosis were observed, the timing of dephosphorylation of the mutant Ki67 (show MKI67 ELISA Kits) in anaphase was delayed, indicating that Ki67 (show MKI67 ELISA Kits) itself is one of the substrates of PP1gamma-Ki67 (show MKI67 ELISA Kits).
the lipin-1 (show LPIN1 ELISA Kits) N-terminal domain is important for its catalytic activity, nuclear localization, and binding to PP-1cgamma
Protein phosphatase 1gamma promotes the alternative splicing of CaMKIIdelta through its interaction with alternative splice factor.
PPP1C (show PPP1CA ELISA Kits) isoforms have distinct contribution to the outside-in alphaIIbbeta3 signalling-dependent functions in HEK293 alphaIIbbeta3 cells.
Findings indicate that phosphatases PP1alpha (show PPP1CA ELISA Kits) and PP1gamma are key regulators of RIG-I (show DDX58 ELISA Kits) and MDA5 (show IFIH1 ELISA Kits) antiviral signaling.
When the Px(T)PxR (show NR1I2 ELISA Kits) motif is deleted or mutated via insertion of a phosphorylation site mimic (T311D), PP-1c fails to bind to all three ASPP proteins, ASPP1 (show PPP1R13B ELISA Kits), ASPP2 (show TP53BP2 ELISA Kits) and iASPP (show PPP1R13L ELISA Kits).
The protein encoded by this gene belongs to the protein phosphatase family, PP1 subfamily. PP1 is an ubiquitous serine/threonine phosphatase that regulates many cellular processes, including cell division. It is expressed in mammalian cells as three closely related isoforms, alpha, beta/delta and gamma, which have distinct localization patterns. This gene encodes the gamma isozyme. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
protein phosphatase 1, catalytic subunit, gamma isoform
, serine/threonine-protein phosphatase PP1-gamma catalytic subunit
, PP1C gamma 1
, PP1C gamma 2
, protein phosphatase 1C catalytic subunit
, serine/threonine phosphatase 1 gamma
, protein serine-threonine phosphatase catalytic subunit PP-1b
, protein phosphatase type 1 catalytic subunit gamma isoform
, protein phosphatase 1 gamma 1
, protein phosphatase 1-gamma 1
, serine/threonine-protein phosphatase PP1-gamma catalytic subunit A